Mercury in PDB 1g0e: Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole

Enzymatic activity of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole

All present enzymatic activity of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole:
4.2.1.1;

Protein crystallography data

The structure of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole, PDB code: 1g0e was solved by D.Duda, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	25.00 / 1.60
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	42.142, 41.490, 72.063, 90.00, 104.28, 90.00
*R / R_free (%)*	17.9 / 20

Other elements in 1g0e:

The structure of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole (pdb code 1g0e). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole, PDB code: 1g0e:

Mercury binding site 1 out of 1 in 1g0e

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Mercury Binding Sites List in 1g0e

Mercury binding site 1 out of 1 in the Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg263 b:12.1 occ:1.00	SG	A:CYS206	2.3	8.8	1.0
	O	A:HOH271	2.4	14.4	1.0
	O	A:GLN137	2.9	6.2	1.0
	CB	A:CYS206	2.9	6.3	1.0
	O	A:GLU205	3.2	5.3	1.0
	O	A:VAL135	3.3	10.1	1.0
	C	A:GLN137	3.4	7.2	1.0
	O	A:HOH375	3.5	18.8	1.0
	O	A:HOH374	3.5	26.4	1.0
	CA	A:CYS206	3.5	4.5	1.0
	C	A:GLU205	3.5	4.8	1.0
	N	A:GLN137	3.7	8.8	1.0
	N	A:CYS206	3.7	4.7	1.0
	C	A:VAL135	3.8	9.2	1.0
	C	A:GLN136	4.0	9.5	1.0
	N	A:PRO138	4.1	6.8	1.0
	CA	A:GLN137	4.1	7.5	1.0
	CA	A:PRO138	4.3	6.4	1.0
	N	A:GLN136	4.3	9.9	1.0
	CA	A:GLN136	4.3	10.5	1.0
	N	A:GLU205	4.3	4.8	1.0
	O	A:HOH369	4.5	16.2	1.0
	CA	A:GLU205	4.5	4.8	1.0
	O	A:GLN136	4.6	9.7	1.0
	CA	A:VAL135	4.6	8.7	1.0
	CB	A:LEU204	4.7	5.7	1.0
	O	A:ALA134	4.9	7.2	1.0
	C	A:LEU204	4.9	4.9	1.0
	C	A:CYS206	5.0	4.1	1.0

Reference:

D.Duda, C.Tu, M.Qian, P.Laipis, M.Agbandje-Mckenna, D.N.Silverman, R.Mckenna. Structural and Kinetic Analysis of the Chemical Rescue of the Proton Transfer Function of Carbonic Anhydrase II. Biochemistry V. 40 1741 2001.
ISSN: ISSN 0006-2960
PubMed: 11327835
DOI: 10.1021/BI002295Z

Page generated: Fri Aug 8 09:01:16 2025

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